The cloning, purification and characterization of a cold active beta-galactosidase from the psychrotolerant Antarctic bacterium Arthrobacter sp. C2-2

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22330%2F03%3A00008940" target="_blank" >RIV/60461373:22330/03:00008940 - isvavai.cz</a>

Result on the web

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DOI - Digital Object Identifier

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Result language

angličtina

Original language name

The cloning, purification and characterization of a cold active beta-galactosidase from the psychrotolerant Antarctic bacterium Arthrobacter sp. C2-2

Original language description

The Gram-positive Antarctic bacterium Arthrobacter sp. C2-2 contains two, possibly three cold-active isoenzymes of beta-galactosidase. The C2-2-1 isoenzyme was cloned, purified and characterised. This beta-galactosidase was classified as being a member of the Family 2 of glycosidases. It is a homotetrameric enzyme, each subunit being composed of 1023 amino acids and it shows great activity towards lactose as a substrate. The C2-2-1 isoenzyme is particularly cold-active, compared to other beta-galactosidases including those from some closely-related bacteria, retaining 20% of activity at 10 .C compared with maximum values. The temperature optimum of the purified enzyme was 40 .C using lactose as the substrate. The enzyme is particularly thermolabile, losing all activity within 10 min at 50 .C. The isoelectric point of the enzyme was 5.9. Dithiothreitol and Mg2+ ions were strong activators, whereas Cu2+, Al3+ and Tris were strong inhibitors of activity. The enzyme exhibited transglycosyl

Czech name

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Czech description

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Type

J_x - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

CEP classification

CE - Biochemistry

OECD FORD branch

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Project

<a href="/en/project/GA204%2F02%2F0843" target="_blank" >GA204/02/0843: Complex cold adaptation study of enzymes on molecular level and their application in biotechnology</a><br>

Continuities

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year

2003

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Enzyme and Microbial Technology

ISSN

0141-0229

e-ISSN

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Volume of the periodical

2003

Issue of the periodical within the volume

33

Country of publishing house

BE - BELGIUM

Number of pages

9

Pages from-to

836-844

UT code for WoS article

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EID of the result in the Scopus database

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